|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
4-337 |
1.71e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 4 DIITNLRCRLKEAEEERLKAAQYglqlvesqNELQNQLDKCRNEMMTMT-ESYEQEKYTLQREVELKSRMLESLSCE--- 79
Cdd:COG1196 193 DILGELERQLEPLERQAEKAERY--------RELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAElae 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 80 CEAIKQQQKMHLEKLEEQLS------RSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSE 153
Cdd:COG1196 265 LEAELEELRLELEELELELEeaqaeeYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 154 RVQESmSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVAN 233
Cdd:COG1196 345 ELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 234 QDLQVQLDQALQ---QALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMKGSQ 310
Cdd:COG1196 424 EELEEALAELEEeeeEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330 340
....*....|....*....|....*..
gi 1045561459 311 TEFEQQERLLAMLEQKNGEIKHLLGEI 337
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-353 |
1.14e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 2 EADIITNLRCRLKEAEeerlkaaqygLQLVESQNELQnQLDKCRNEMMTMTESYEQEKYTLQREVELKSRmLESLSCECE 81
Cdd:TIGR02168 163 EAAGISKYKERRKETE----------RKLERTRENLD-RLEDILNELERQLKSLERQAEKAERYKELKAE-LRELELALL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 82 AIK-QQQKMHLEKLEEQLSRShGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDH-QKELLSCKSE------ELRVMSE 153
Cdd:TIGR02168 231 VLRlEELREELEELQEELKEA-EEELEELTAELQELEEKLEELRLEVSELEEEIEElQKELYALANEisrleqQKQILRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 154 RvQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKeekeerekeavsyyNALEKARVAN 233
Cdd:TIGR02168 310 R-LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE--------------AELEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 234 QDLQVQLDQAlqqaldpnskgNSLFAEVEDRRAAMERQLISMKVKYQSLKKqNVFNREQMQRMKLQIATLLQMKGSQTEF 313
Cdd:TIGR02168 375 EELEEQLETL-----------RSKVAQLELQIASLNNEIERLEARLERLED-RRERLQQEIEELLKKLEEAELKELQAEL 442
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1045561459 314 EQQERLLAMLEQKNGEIKHLLGEIRN-LEKFKNLYDSMESK 353
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREeLEEAEQALDAAERE 483
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
22-439 |
2.81e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 22 KAAQYGLQLVESQNELQNQLDKCRNEMMTMtESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQKMHLEKLeeQLSRS 101
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKMTL-ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL--QHLKN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 102 HGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSckseelrvmservQESMSSEmlALQIEltemesmKTTLK 181
Cdd:pfam15921 539 EGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG-------------QHGRTAG--AMQVE-------KAQLE 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 182 EEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEv 261
Cdd:pfam15921 597 KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED- 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 262 edrraamerqlismkvkYQSLKKQNVFNREQMQRMKLQIAtlLQMKGSQTEFEQQERLLAMLEQKNGE-IKHLLGEIRNL 340
Cdd:pfam15921 676 -----------------YEVLKRNFRNKSEEMETTTNKLK--MQLKSAQSELEQTRNTLKSMEGSDGHaMKVAMGMQKQI 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 341 EKFKNLYDSMESKPSVDSGTLEDNTYYTDLLQMKLDNLNKEIEST-------KGELSIQRMKALFESQRALDIERKLfaN 413
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVateknkmAGELEVLRSQERRLKEKVANMEVAL--D 814
|
410 420
....*....|....*....|....*.
gi 1045561459 414 ERCLQLSESENMKLRAKLDELKLKYE 439
Cdd:pfam15921 815 KASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
12-208 |
3.51e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 12 RLKEAEEERLKA-AQYGL--QLVESQNELQNQLDKCR--NEMMTMTESY--EQEKYTLQREVELKSRMLESLSCECEAIK 84
Cdd:COG4913 236 DLERAHEALEDArEQIELlePIRELAERYAAARERLAelEYLRAALRLWfaQRRLELLEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 85 QQ---QKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQ---ES 158
Cdd:COG4913 316 ARldaLREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAallEA 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1045561459 159 MSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRL 208
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
6-339 |
4.95e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 6 ITNLRCRLKEAEEERLKAAqyglqlvESQNELQNQLDKCRNEmmtmTESYEQEKYTLQREVELKSRMLESLSCECEAIKQ 85
Cdd:TIGR02168 672 ILERRREIEELEEKIEELE-------EKIAELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 86 QQkmhlEKLEEQLSRSHgQEVNELKTKIEKLKVELDEARLSEKQLkhqvdhqkellscksEELRVMSERVQESMSSEMLA 165
Cdd:TIGR02168 741 EV----EQLEERIAQLS-KELTELEAEIEELEERLEEAEEELAEA---------------EAEIEELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 166 LQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKE----EKEEREKEAVS------YYNALEKARVANQD 235
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEqieeLSEDIESLAAEieeleeLIEELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 236 LQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLismkvkyQSLKKQNVFNREQMQRMKLQIATLLQM--KGSQTEF 313
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRREL-------EELREKLAQLELRLEGLEVRIDNLQERlsEEYSLTL 953
|
330 340
....*....|....*....|....*.
gi 1045561459 314 EQQERLLAMLEQKNGEIKHLLGEIRN 339
Cdd:TIGR02168 954 EEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
56-268 |
7.46e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 7.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 56 EQEKYTLQREVELKSRMLESLSCECEAIKQQqkmhLEKLEEQLSRSHgQEVNELKTKIEKLKVELDEARLSEKQLKHQVD 135
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALA-RRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 136 HQKELLScksEELRVM--------------------SERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLE 195
Cdd:COG4942 101 AQKEELA---ELLRALyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1045561459 196 LLITNLMRQVDRLKEEKEEREKeavsyynALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAM 268
Cdd:COG4942 178 ALLAELEEERAALEALKAERQK-------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
6-437 |
2.74e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 6 ITNLRCRLKEAEEERLKAAQYGLQ-LVESQNELQnQLDKCRNEMMTMTESYEQEKYTLQREVELKSRMLESLSCECEAIK 84
Cdd:pfam15921 87 VKDLQRRLNESNELHEKQKFYLRQsVIDLQTKLQ-EMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDML 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 85 QQQKMHLEKLEEQLsRSHGQEVNELKTkiekLKVELDEArlSEKQLKHQVD----HQKELLSCKSEELRvmservqeSMS 160
Cdd:pfam15921 166 EDSNTQIEQLRKMM-LSHEGVLQEIRS----ILVDFEEA--SGKKIYEHDSmstmHFRSLGSAISKILR--------ELD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 161 SEMLALQIELTEMESMKTTLKEEvnelqyRQEQLELLitnLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQL 240
Cdd:pfam15921 231 TEISYLKGRIFPVEDQLEALKSE------SQNKIELL---LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 241 DQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKY----QSLKKQNVFNREQMQRMKLQIATLLQMKGSQTefEQQ 316
Cdd:pfam15921 302 EIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYedkiEELEKQLVLANSELTEARTERDQFSQESGNLD--DQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 317 ERLLAMLEQKNGE---------------------IKHLLGEI--RNLE--KFKNLYDSMESKPsvdSGTLEDNTYY---- 367
Cdd:pfam15921 380 QKLLADLHKREKElslekeqnkrlwdrdtgnsitIDHLRRELddRNMEvqRLEALLKAMKSEC---QGQMERQMAAiqgk 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1045561459 368 TDLLQmKLDNLNKEIESTK-------GELSIQRMkALFESQRAL-DIERKLFANERCLQLSESENMKLRAKLDeLKLK 437
Cdd:pfam15921 457 NESLE-KVSSLTAQLESTKemlrkvvEELTAKKM-TLESSERTVsDLTASLQEKERAIEATNAEITKLRSRVD-LKLQ 531
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
28-283 |
4.48e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 28 LQLVESQNELQNQLDKCRNEMmtmtESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQ---KMHLEKLEEQLSrSHGQ 104
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSEL----RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEeklKERLEELEEDLS-SLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 105 EVNELKTKIEKLKVELDEARLSEKQLKHQV-DHQKELLSCKSEELRVMSERVQESMSSEMLALQ---IELTEMESMKTTL 180
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 181 KEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAE 260
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260
....*....|....*....|...
gi 1045561459 261 VEDRRAAMERQLISMKVKYQSLK 283
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELS 934
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
15-342 |
7.49e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 15 EAEEERLKAAQYGLQLVESQNELQNQLDKCRNEMMTMTESYEQEKYTLQREVELKSRmLESLSCECEAIKQQQKMHLEKL 94
Cdd:COG4717 108 EAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE-LEELEAELAELQEELEELLEQL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 95 ---EEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESMSSEMLALQ---- 167
Cdd:COG4717 187 slaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLglgg 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 168 ---------------------IELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNAL 226
Cdd:COG4717 267 sllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 227 EKARVANQDLQVQLDQALQQALdpNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLkkqnvfnREQMQRMKLQIATLLQM 306
Cdd:COG4717 347 EELQELLREAEELEEELQLEEL--EQEIAALLAEAGVEDEEELRAALEQAEEYQEL-------KEELEELEEQLEELLGE 417
|
330 340 350
....*....|....*....|....*....|....*.
gi 1045561459 307 KGSQTEFEQQERLLAMLEQKNGEIKHLLGEIRNLEK 342
Cdd:COG4717 418 LEELLEALDEEELEEELEELEEELEELEEELEELRE 453
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
36-342 |
8.27e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 36 ELQNQLDKCRNEMMTMTESYEQekytLQREVELKSRMLESLSCECEAIKQQQKMHLEKLEEQLSrSHGQEVNELKTKIEK 115
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIER----LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGY-ELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 116 LKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLE 195
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 196 LLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAME---RQL 272
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklkREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 273 ISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQ--------MKGSQTEFEQQE----RLLAMLEQKNGEIKHLLGEIRNL 340
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAkineleeeKEDKALEIKKQEwkleQLAADLSKYEQELYDLKEEYDRV 481
|
..
gi 1045561459 341 EK 342
Cdd:TIGR02169 482 EK 483
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
23-316 |
2.48e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 23 AAQYGLQLVESQNELQNQLDKcrnemMTMTESYEQEKYTLQREVELKSRMLESlsceceaiKQQQKMHLEKLEEQLSRSH 102
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDA-----LNKQKLLEAEDKLVQQDLEQTLALLDK--------IDRQKEETEQLKQQLAQAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 103 gQEVNELKTKIEKLKVELDE------ARLSEKQLKHQV--------DHQKELLSCKSE--ELRVMSERVQESMSSEMLAL 166
Cdd:PRK11281 94 -AKLRQAQAELEALKDDNDEetretlSTLSLRQLESRLaqtldqlqNAQNDLAEYNSQlvSLQTQPERAQAALYANSQRL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 167 QiELTEM-----ESMKTTLKEEVNELQYRQEQLELLI---TNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDL-- 236
Cdd:PRK11281 173 Q-QIRNLlkggkVGGKALRPSQRVLLQAEQALLNAQNdlqRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAin 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 237 -------QVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVfnreqmqRMKLQIATLLQmkgS 309
Cdd:PRK11281 252 skrltlsEKTVQEAQSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTLTQQNL-------RVKNWLDRLTQ---S 321
|
....*..
gi 1045561459 310 QTEFEQQ 316
Cdd:PRK11281 322 ERNIKEQ 328
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
28-351 |
2.53e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 28 LQLVESQNELQNQLDKCRNEMMTMtESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQKMHLEklEEQLSRSHGQEVN 107
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 108 ELKTKIEKLKVEldeaRLSEKQLKHQVDHQKELLSCKSEELRvMSERVQESMSSemlALQIELTEMESMKTTLKEEVNEL 187
Cdd:pfam17380 352 RIRQEERKRELE----RIRQEEIAMEISRMRELERLQMERQQ-KNERVRQELEA---ARKVKILEEERQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 188 QYRQEQLELlitnLMRQVDRLKEEKEERekeavsyynaLEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAA 267
Cdd:pfam17380 424 QIRAEQEEA----RQREVRRLEEERARE----------MERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 268 ME--RQLISMKVKYqslKKQNVFNREQMQRMKLQiatllQMKGSQTE-FEQQERLLAMLEQKNG----EIKHLLGEIRNL 340
Cdd:pfam17380 490 EEqrRKILEKELEE---RKQAMIEEERKRKLLEK-----EMEERQKAiYEEERRREAEEERRKQqemeERRRIQEQMRKA 561
|
330
....*....|.
gi 1045561459 341 EKFKNLYDSME 351
Cdd:pfam17380 562 TEERSRLEAME 572
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
91-307 |
4.45e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 91 LEKLEEQlsRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQK-ELLSCKSEELRVMSERVQEsmssEMLALQIE 169
Cdd:COG4913 244 LEDAREQ--IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEA----ELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 170 LTEMESMKTTLKEEVNELQYRQ-EQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQAL 248
Cdd:COG4913 318 LDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1045561459 249 DPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMK 307
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD 456
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-201 |
5.06e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 2 EADIITNLRCRLKEAEEERlkaaqygLQLVESQNELQNQLDKCRnemmTMTESYEQEKYTLQREVELKSRMLESLSCECE 81
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEI-------EELEAQIEQLKEELKALR----EALDELRAELTLLNEEAANLRERLESLERRIA 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 82 AIKQQqkmhLEKLEEQLSRshgqevneLKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERvQESMSS 161
Cdd:TIGR02168 835 ATERR----LEDLEEQIEE--------LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE-LEELSE 901
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1045561459 162 EMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNL 201
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
29-336 |
6.07e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 29 QLVESQNELQNQLDKCRNEMMTMTESYEQEKYTLQREVELKSRMLESLSceceaIKQQQKMHLEKLEEQLSRSHGQEVNE 108
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP-----NLQNITVRLQDLTEKLSEAEDMLACE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 109 LKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESMSS----EMLALQI---ELTEMESMKTTLK 181
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSirvlPKELLASrqlALQKMQSEKEQLT 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 182 EEVNELQYRQEQLELLITNLmRQVDRLKEEKEEREKEAVSYYNalekarvANQDLQVQLDQALQQALDPNSKGNSLFAEV 261
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHI-EEYDREFNEIENASSSLGSDLA-------AREDALNQSLKELMHQARTVLKARTEAHFN 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 262 EDRRAAMERQLISmkvKYQSLKKQNVFNREQMQRMKLQIATL----------------LQMKGSQTEFEQQERLLAMLEQ 325
Cdd:TIGR00618 766 NNEEVTAALQTGA---ELSHLAAEIQFFNRLREEDTHLLKTLeaeigqeipsdedilnLQCETLVQEEEQFLSRLEEKSA 842
|
330
....*....|.
gi 1045561459 326 KNGEIKHLLGE 336
Cdd:TIGR00618 843 TLGEITHQLLK 853
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
96-349 |
7.55e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 96 EQLSRSHgQEVNELKTKIEKLKvELDEARLSEKQLKHQVDHQKELLSckseelRVMSERVQEsmssEMLALQIELTEMES 175
Cdd:COG4913 235 DDLERAH-EALEDAREQIELLE-PIRELAERYAAARERLAELEYLRA------ALRLWFAQR----RLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 176 MKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKeekeerekeavsyYNALEkarvanqDLQVQLDQALQQAldpnskgn 255
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNG-------------GDRLE-------QLEREIERLEREL-------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 256 slfAEVEDRRAAMERQLismkvkyQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTE--FEQQERLLAMLEQKNGEIKHL 333
Cdd:COG4913 355 ---EERERRRARLEALL-------AALGLPLPASAEEFAALRAEAAALLEALEEELEalEEALAEAEAALRDLRRELREL 424
|
250
....*....|....*.
gi 1045561459 334 LGEIRNLEKFKNLYDS 349
Cdd:COG4913 425 EAEIASLERRKSNIPA 440
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
85-256 |
2.12e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 85 QQQKMHLEKLEEQLSRSHgQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELR--------------- 149
Cdd:COG3883 26 SELQAELEAAQAELDALQ-AELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyrsggsvsy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 150 -----------------VMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEK 212
Cdd:COG3883 105 ldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1045561459 213 EEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNS 256
Cdd:COG3883 185 AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
17-402 |
2.34e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 17 EEERLKAAQyglqlVESQNELQNQLDKCRNEMMT-MTESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQKMHLEKLE 95
Cdd:pfam05483 264 EESRDKANQ-----LEEKTKLQDENLKELIEKKDhLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQME 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 96 E--QLSRSHGQEVNELKTKIEKLKVELdeaRLSEKQLKHQVDHQKEL---LSCKSEELRVMSeRVQESMSSEMLALQIEL 170
Cdd:pfam05483 339 ElnKAKAAHSFVVTEFEATTCSLEELL---RTEQQRLEKNEDQLKIItmeLQKKSSELEEMT-KFKNNKEVELEELKKIL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 171 TEMESM---KTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEkarvanqDLQVQLDQALQQA 247
Cdd:pfam05483 415 AEDEKLldeKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVE-------DLKTELEKEKLKN 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 248 LDPNSKGNSLFaeVEDRRAAMERQLISMKVKYQSLKKQNvfNREQMQRMKLQIATLLqmkgsqtefEQQERLLAMLEQKN 327
Cdd:pfam05483 488 IELTAHCDKLL--LENKELTQEASDMTLELKKHQEDIIN--CKKQEERMLKQIENLE---------EKEMNLRDELESVR 554
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1045561459 328 GEIKHLLGEIR-NLEKFKNLYDSMESKPSVDSGTLEDNTYYTDLLQMKLDNLNKEIESTKGELSIQRMKALFESQR 402
Cdd:pfam05483 555 EEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ 630
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
91-267 |
2.71e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 91 LEKLEEQLSRShGQEVNELKTKIEKLKVELD---EARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQ-ESMSSEMLAL 166
Cdd:COG4913 612 LAALEAELAEL-EEELAEAEERLEALEAELDalqERREALQRLAEYSWDEIDVASAEREIAELEAELERlDASSDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 167 QIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVAN-------QDLQVQ 239
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAalgdaveRELREN 770
|
170 180
....*....|....*....|....*...
gi 1045561459 240 LDQALQQAldpNSKGNSLFAEVEDRRAA 267
Cdd:COG4913 771 LEERIDAL---RARLNRAEEELERAMRA 795
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
6-434 |
4.37e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 6 ITNLRCRLKEAEEErLKAAQYGL--------QLVESQNELQNQLDKCRNEM---MTMTESYEQEKYTLQREVE-LKSRML 73
Cdd:pfam01576 231 IAELRAQLAKKEEE-LQAALARLeeetaqknNALKKIRELEAQISELQEDLeseRAARNKAEKQRRDLGEELEaLKTELE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 74 ESLSC-----ECEAIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCK---- 144
Cdd:pfam01576 310 DTLDTtaaqqELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESEnael 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 145 SEELRVMSERVQES------MSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEkeereke 218
Cdd:pfam01576 390 QAELRTLQQAKQDSehkrkkLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD------- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 219 avsyynaLEKARVANQDLQVQLDQALQQALDPNSKGNSLfaevEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKL 298
Cdd:pfam01576 463 -------VSSLESQLQDTQELLQEETRQKLNLSTRLRQL----EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 299 QiatLLQMKGSQTEFEQ-QERLLAMLEQKNGEIKHLLGEIRNLEKFKNLYDSMESKPSVDSGTLEDNTYYTDLLQMKLDN 377
Cdd:pfam01576 532 K---LEEDAGTLEALEEgKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQ 608
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045561459 378 LNKEIESTKGELSIQRMKALFESQ----RALDIERKLFANERCLQLSESENMKLRAKLDEL 434
Cdd:pfam01576 609 MLAEEKAISARYAEERDRAEAEAReketRALSLARALEEALEAKEELERTNKQLRAEMEDL 669
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
12-197 |
5.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 12 RLKEAEEErLKAAQyglQLVESQNELQNQLDKCRNEMmtmtESYEQEKYTLQREVELKSRMLESLSCECEaiKQQQKMHL 91
Cdd:COG4717 72 ELKELEEE-LKEAE---EKEEEYAELQEELEELEEEL----EELEAELEELREELEKLEKLLQLLPLYQE--LEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 92 EKLEEQLS--RSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKEllscksEELRVMSERVQEsMSSEMLALQIE 169
Cdd:COG4717 142 AELPERLEelEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE------EELQDLAEELEE-LQQRLAELEEE 214
|
170 180
....*....|....*....|....*...
gi 1045561459 170 LTEMESMKTTLKEEVNELQYRQEQLELL 197
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALE 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
37-285 |
5.17e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 37 LQNQLDKCRNEMMTMTESYEQEKYTLQREVELKSRMLESLsceceaikqQQKMHLEKLEEQLSrSHGQEVNELKTKIEKL 116
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEF---------RQKNGLVDLSEEAK-LLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 117 KVELDEARLSEKQLKHQVDHQKELLSckseelRVMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLEL 196
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALP------ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 197 LITNLMRQVdrlkeekeerekeAVSYYNALEKARVANQDLQVQLDQALQQALDpnskgnslFAEVEDRRAAMERQLISMK 276
Cdd:COG3206 306 QLQQEAQRI-------------LASLEAELEALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVAR 364
|
....*....
gi 1045561459 277 VKYQSLKKQ 285
Cdd:COG3206 365 ELYESLLQR 373
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
9-199 |
5.58e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 39.67 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 9 LRCRLKEAEEERLKAAQyglQLVESQNELQNQLDkcrnemmtmtesyEQEKYTLQREVELKSRMLESLSCECEAIKQQQK 88
Cdd:pfam05622 294 LRLGQEGSYRERLTELQ---QLLEDANRRKNELE-------------TQNRLANQRILELQQQVEELQKALQEQGSKAED 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 89 MHL--EKLEEQLsrshgQEVNELKTKIEKLKVELDEARLSEKQLKHQ-VDHQKELLSCKSEELRVMSER----------- 154
Cdd:pfam05622 358 SSLlkQKLEEHL-----EKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEERykkyvekaksv 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1045561459 155 -------VQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLIT 199
Cdd:pfam05622 433 iktldpkQNPASPPEIQALKNQLLEKDKKIEHLERDFEKSKLQREQEEKLIV 484
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
104-213 |
5.95e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 104 QEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEEL-RVMSERvqesmssEMLALQIELTEMESMKTTLKE 182
Cdd:COG1579 38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgNVRNNK-------EYEALQKEIESLKRRISDLED 110
|
90 100 110
....*....|....*....|....*....|.
gi 1045561459 183 EVNELQYRQEQLELLITNLMRQVDRLKEEKE 213
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELE 141
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
112-303 |
6.84e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.98 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 112 KIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESmSSEMLALQIELTEMESMKTTLKEEVNELQYRQ 191
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL-ARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 192 EQLELLITNLMRQVDR----------LKEEKEEREKEAVSYYNALEKARVAN----QDLQVQLDQALQQALDPNSKGNSL 257
Cdd:COG4942 100 EAQKEELAELLRALYRlgrqpplallLSPEDFLDAVRRLQYLKYLAPARREQaeelRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1045561459 258 FAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATL 303
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
12-186 |
8.18e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 12 RLKEAEEERLKAAQygLQLVESQNELQNQLDKCRNEMMTMTESYEQE-------KYTLQREVELKSRMLESLSCECEAIK 84
Cdd:PTZ00121 1611 EAKKAEEAKIKAEE--LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAeeenkikAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 85 QQQKMHLEKLE-----EQLSRSHGQEvnelKTKIEKLKVELDEARLSEKQLKHQVDHQKEllscKSEELRVMSE---RVQ 156
Cdd:PTZ00121 1689 KAAEALKKEAEeakkaEELKKKEAEE----KKKAEELKKAEEENKIKAEEAKKEAEEDKK----KAEEAKKDEEekkKIA 1760
|
170 180 190
....*....|....*....|....*....|
gi 1045561459 157 ESMSSEMLALQIELTEMESMkttLKEEVNE 186
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAV---IEEELDE 1787
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
106-439 |
8.49e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 106 VNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEElRVMSERVQesmssemlALQIELTEMEsmkttLKEEVN 185
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQ--------ALLKEKREYE-----GYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 186 ELQYRQEQLEllitNLMRQVDRLKEEkeerekeavsyynaLEKARVANQDLQVQLDQALQQALDPNSKgnsLFAEVEDRR 265
Cdd:TIGR02169 231 EKEALERQKE----AIERQLASLEEE--------------LEKLTEEISELEKRLEEIEQLLEELNKK---IKDLGEEEQ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 266 AAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTEfeQQERLLAMLEQKNGEIKHLLGEIRNLEKFKN 345
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA--EIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 346 LYDSMESKPSVDSGTLEDNTyytDLLQMKLDNLNKEIESTKGELSIQRMKALFESQRALDIERKLFANERCLQLSESENM 425
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDEL---KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKE 444
|
330
....*....|....
gi 1045561459 426 KLRAKLDELKLKYE 439
Cdd:TIGR02169 445 DKALEIKKQEWKLE 458
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
53-272 |
9.27e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 53 ESYEQEKYTLQREVELksrmLESLSCECEAIKQ--QQKMHLEKLEEQLSRSHGQevnelkTKIEKLKVELDEARLSEKQL 130
Cdd:COG4913 238 ERAHEALEDAREQIEL----LEPIRELAERYAAarERLAELEYLRAALRLWFAQ------RRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1045561459 131 KHQVDHQKELLSCKSEELRVMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLI-------TNLMR 203
Cdd:COG4913 308 EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaeefAALRA 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1045561459 204 QVDRLKEEKEEREKEAVsyyNALEKARVANQDLQVQLDQALQ--QALDpnSKGNSLFAEVEDRRAAMERQL 272
Cdd:COG4913 388 EAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAeiASLE--RRKSNIPARLLALRDALAEAL 453
|
|
| |
